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dc.contributor.authorHe, Xu
dc.contributor.authorHaselhorst, Thomas
dc.contributor.authorvon Itzstein, Mark
dc.contributor.authorKolarich, Daniel
dc.contributor.authorPacker, Nicolle H
dc.contributor.authorGloster, Tracey M
dc.contributor.authorVocadlo, David J
dc.contributor.authorClarke, Lorne A
dc.contributor.authorQian, Yi
dc.contributor.authorKermode, Allison R
dc.date.accessioned2017-05-05T00:32:33Z
dc.date.available2017-05-05T00:32:33Z
dc.date.issued2012
dc.date.modified2013-06-17T02:37:23Z
dc.identifier.issn2041-1723
dc.identifier.doi10.1038/ncomms2070
dc.identifier.urihttp://hdl.handle.net/10072/48288
dc.description.abstractLysosomal storage diseases are a class of over 70 rare genetic diseases that are amenable to enzyme replacement therapy. Towards developing a plant-based enzyme replacement therapeutic for the lysosomal storage disease mucopolysaccharidosis I, here we expressed a-L-iduronidase in the endosperm of maize seeds by a previously uncharacterized mRNA-targeting-based mechanism. Immunolocalization, cellular fractionation and in situ RT-PCR demonstrate that the a-L-iduronidase protein and mRNA are targeted to endoplasmic reticulum (ER)-derived protein bodies and to protein body-ER regions, respectively, using regulatory (5'- and 3'-UTR) and signal-peptide coding sequences from the ?-zein gene. The maize a-L-iduronidase exhibits high activity, contains high-mannose N-glycans and is amenable to in vitro phosphorylation. This mRNA-based strategy is of widespread importance as plant N-glycan maturation is controlled and the therapeutic protein is generated in a native form. For our target enzyme, the N-glycan structures are appropriate for downstream processing, a prerequisite for its potential as a therapeutic protein.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherNature Publishing Group
dc.publisher.placeUnited Kingdom
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom1062-1
dc.relation.ispartofpageto1062-9
dc.relation.ispartofjournalNature Communications
dc.relation.ispartofvolume3
dc.rights.retentionY
dc.subject.fieldofresearchEnzymes
dc.subject.fieldofresearchcode310106
dc.titleProduction of α-L-iduronidase in maize for the potential treatment of a human lysosomal storage disease
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.date.issued2012
gro.hasfulltextNo Full Text
gro.griffith.authorvon Itzstein, Mark
gro.griffith.authorHaselhorst, Thomas E.
gro.griffith.authorKolarich, Daniel
gro.griffith.authorPacker, Nicki


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